Aeen Ebrahim Amini

Sep 12, 2024 | journals.plos.org | Temerty Faculty |Genki Amano |Erica Stuart |Aeen Ebrahim Amini |PLOS Pathogens

Loading metrics Open Access Peer-reviewedResearch Article Citation: So RWL, Amano G, Stuart E, Ebrahim Amini A, Aguzzi A, Collingridge GL, et al. (2024) α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model. PLoS Pathog 20(9): e1012517. https://doi.org/10.1371/journal.ppat.1012517Editor: Suzette A.

Mar 30, 2024 | biorxiv.org | Erica Stuart |Adriano Aguzzi |Raphaella W.L. So |Aeen Ebrahim Amini

AbstractThe cellular prion protein, PrPC, has been postulated to function as a receptor for α-synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of α-synuclein aggregates in neurodegenerative disorders such as Parkinson's disease. To test this hypothesis, we compared the propagation behavior of two different α-synuclein aggregate strains in M83 transgenic mice that either expressed or did not express PrPC.